2L23

NMR structure of the ACID (ACtivator Interacting Domain) of the human mediator Med25 protein

Summary for 2L23

• Entry DOI: 10.2210/pdb2l23/pdb
• Descriptor: Mediator of RNA polymerase II transcription subunit 25 (1 entity in total)
• Functional Keywords: human mediator complex, pancreatic tumor overexpressed domain, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q71SY5
• Total number of polymer chains: 1
• Total formula weight: 19220.33

Authors

Bontems, F.,Monte, D.,Dewitte, F.,Villeret, V. (deposition date: 2010-08-10, release date: 2010-11-24, Last modification date: 2024-05-22)

Primary citation

Bontems, F.,Verger, A.,Dewitte, F.,Lens, Z.,Baert, J.L.,Ferreira, E.,Launoit, Y.,Sizun, C.,Guittet, E.,Villeret, V.,Monte, D.
NMR structure of the human Mediator MED25 ACID domain.
J.Struct.Biol., 174:245-251, 2011

PubMed Abstract: MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts with VP16 through a central MED25 PTOV (Prostate tumour overexpressed)/ACID (Activator interacting domain) domain of unknown structure. As a first step towards understanding the mechanism of recruitment of transactivation domains by MED25, we report here the NMR structure of the MED25 ACID domain. The domain architecture consists of a closed β-barrel with seven strands (Β1-Β7) and three α-helices (H1-H3), an architecture showing similarities to that of the SPOC (Spen paralog and ortholog C-terminal domain) domain-like superfamily. Preliminary NMR chemical shift mapping showed that VP16 H2 (VP16C) interacts with MED25 ACID through one face of the β-barrel, defined by strands B4-B7-B6.

PubMed: 20974256
DOI: 10.1016/j.jsb.2010.10.011

Experimental method

SOLUTION NMR